A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome

dc.contributor.authorPeng, Zhenling
dc.contributor.authorOldfield, Christopher J.
dc.contributor.authorXue, Bin
dc.contributor.authorMizianty, Marcin J.
dc.contributor.authorDunker, A. Keith
dc.contributor.authorKurgan, Lukasz
dc.contributor.authorUversky, Vladimir N.
dc.contributor.departmentBiochemistry and Molecular Biology, School of Medicineen_US
dc.date.accessioned2022-03-31T16:22:49Z
dc.date.available2022-03-31T16:22:49Z
dc.date.issued2013-08-13
dc.descriptionThis article is made available for unrestricted research re-use and secondary analysis in any form or be any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.en_US
dc.description.abstractIntrinsic disorder (i.e., lack of a unique 3-D structure) is a common phenomenon, and many biologically active proteins are disordered as a whole, or contain long disordered regions. These intrinsically disordered proteins/regions constitute a significant part of all proteomes, and their functional repertoire is complementary to functions of ordered proteins. In fact, intrinsic disorder represents an important driving force for many specific functions. An illustrative example of such disorder-centric functional class is RNA-binding proteins. In this study, we present the results of comprehensive bioinformatics analyses of the abundance and roles of intrinsic disorder in 3,411 ribosomal proteins from 32 species. We show that many ribosomal proteins are intrinsically disordered or hybrid proteins that contain ordered and disordered domains. Predicted globular domains of many ribosomal proteins contain noticeable regions of intrinsic disorder. We also show that disorder in ribosomal proteins has different characteristics compared to other proteins that interact with RNA and DNA including overall abundance, evolutionary conservation, and involvement in protein–protein interactions. Furthermore, intrinsic disorder is not only abundant in the ribosomal proteins, but we demonstrate that it is absolutely necessary for their various functions.en_US
dc.identifier.citationPeng Z, Oldfield CJ, Xue B, Mizianty MJ, Dunker AK, Kurgan L, Uversky VN. A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome. Cell Mol Life Sci. 2014 Apr;71(8):1477-504. doi: 10.1007/s00018-013-1446-6. Epub 2013 Aug 13. PMID: 23942625; PMCID: PMC7079807.en_US
dc.identifier.urihttps://hdl.handle.net/1805/28356
dc.language.isoen_USen_US
dc.publisherSpringeren_US
dc.relation.isversionof10.1007/s00018-013-1446-6en_US
dc.relation.journalCellular and Molecular Life Sciencesen_US
dc.rightsPublic Health Emergencyen_US
dc.sourcePMCen_US
dc.subjectIntrinsically disordered proteinen_US
dc.subjectMoonlighting proteinen_US
dc.subjectProtein–protein interactionen_US
dc.subjectProtein–RNA interactionen_US
dc.subjectRibosomal proteinsen_US
dc.titleA creature with a hundred waggly tails: intrinsically disordered proteins in the ribosomeen_US
dc.typeArticleen_US
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